HEADER HYDROLASE 23-APR-99 1QGE
TITLE NEW CRYSTAL FORM OF PSEUDOMONAS GLUMAE (FORMERLY CHROMOBACTERIUM
TITLE 2 VISCOSUM ATCC 6918) LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (TRIACYLGLYCEROL HYDROLASE);
COMPND 3 CHAIN: D;
COMPND 4 EC: 3.1.1.3;
COMPND 5 OTHER_DETAILS: CHAIN BREAK FROM V 220 - G 222;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTEIN (TRIACYLGLYCEROL HYDROLASE);
COMPND 8 CHAIN: E;
COMPND 9 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA GLUMAE;
SOURCE 3 ORGANISM_TAXID: 337;
SOURCE 4 STRAIN: CHROMOBACTERIUM VISCOSUM;
SOURCE 5 ATCC: 6918;
SOURCE 6 COLLECTION: 6918;
SOURCE 7 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 8 OTHER_DETAILS: ATCC;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: BURKHOLDERIA GLUMAE;
SOURCE 11 ORGANISM_TAXID: 337;
SOURCE 12 STRAIN: CHROMOBACTERIUM VISCOSUM;
SOURCE 13 ATCC: 6918;
SOURCE 14 COLLECTION: 6918;
SOURCE 15 CELLULAR_LOCATION: EXTRACELLULAR;
SOURCE 16 OTHER_DETAILS: ATCC
KEYWDS PSEUDOMONADACEAE, CIS-PEPTIDE, CLOSED CONFORMATION, HYDROLASE, LID
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.LANG,P.STADLER,A.KOVACS,F.PALTAUF,B.W.DIJKSTRA
REVDAT 5 16-AUG-23 1QGE 1 REMARK
REVDAT 4 27-NOV-19 1QGE 1 JRNL
REVDAT 3 13-JUL-11 1QGE 1 VERSN
REVDAT 2 24-FEB-09 1QGE 1 VERSN
REVDAT 1 06-MAY-99 1QGE 0
JRNL AUTH D.A.LANG,P.STADLER,A.KOVACS,F.PALTAUF,B.W.DIJKSTRA
JRNL TITL STRUCTURAL AND KINETIC INVESTIGATIONS OF ENANTIOMERIC
JRNL TITL 2 BINDING MODE OF SUBCLASS I LIPASES FROM THE FAMILY OF
JRNL TITL 3 PSEUDOMONADACEAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.LANG,B.HOFMANN,L.HAALCK,H.J.HECHT,F.SPENER,R.D.SCHMID,
REMARK 1 AUTH 2 D.SCHOMBURG
REMARK 1 TITL CRYSTAL STRUCTURE OF A BACTERIAL LIPASE FROM CHROMOBACTERIUM
REMARK 1 TITL 2 VISCOSUM ATCC 6918 REFINED AT 1.6 ANGSTROMS RESOLUTION.
REMARK 1 REF J.MOL.BIOL. V. 259 704 1996
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 8683577
REMARK 1 DOI 10.1006/JMBI.1996.0352
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.E.NOBLE,A.CLEASBY,L.N.JOHNSON,M.R.EGMOND,L.G.FRENKEN
REMARK 1 TITL THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM
REMARK 1 TITL 2 PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC
REMARK 1 TITL 3 ASPARTATE.
REMARK 1 REF FEBS LETT. V. 331 123 1993
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 8405390
REMARK 1 DOI 10.1016/0014-5793(93)80310-Q
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 28058
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2315
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 324
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.008 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.025 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.047 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.104 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.171 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.263 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : 12.200; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.959 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.495 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.193 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.817 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE DISORDERED REGION (VAL 220, LEU 221
REMARK 3 AND GLY 223) WAS NOT MODELED OR REFINED.
REMARK 4
REMARK 4 1QGE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000931.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-96
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28124
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1CVL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 10 % PEG
REMARK 280 6000, 5 % PEG 1000, 100 MM HEPES BUFFER, PH 7.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 20.49000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.34500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.67500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.34500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.49000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.67500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 PARTLY DEGRADED LIPASE AS A RESULT OF UNSPECIFIC
REMARK 400 PROTEOLYTIC DIGESTION DURING PURIFICATION AND/OR STORAGE
REMARK 400 PROVEN BY MALDI-TOF MASS SPECTROSCOPY MOLECULAR WEIGHT:
REMARK 400 CALCULATED -- 33091 DALTON, MEASURED -- 32839 DALTON
REMARK 400
REMARK 400 NO OXYANION LOOP FORMATION, BUT A SLIGHT MOVEMENT OF THE
REMARK 400 LID REGION ALREADY OCCURED. THE STRUCTURE STILL REPRESENTS
REMARK 400 THE CLOSED, INACTIVE CONFORMATIONAL STATES OF THE LIPASE
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL D 220
REMARK 465 LEU D 221
REMARK 465 GLY D 222
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP E 241 CB - CG - OD1 ANGL. DEV. = 11.2 DEGREES
REMARK 500 ASP E 241 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG E 257 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 GLN E 291 O - C - N ANGL. DEV. = -16.4 DEGREES
REMARK 500 ARG E 296 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG E 313 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS D 22 151.21 -43.60
REMARK 500 GLN D 53 -77.90 -93.22
REMARK 500 SER D 87 -130.27 54.72
REMARK 500 GLN E 291 -162.86 -113.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN E 291 LEU E 292 -67.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLN E 291 -17.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 320 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 241 OD2
REMARK 620 2 ASP E 287 OD1 170.8
REMARK 620 3 GLN E 291 O 85.7 101.1
REMARK 620 4 VAL E 295 O 95.5 92.9 66.7
REMARK 620 5 HOH E 321 O 88.2 84.0 105.9 171.4
REMARK 620 6 HOH E 330 O 92.8 82.4 164.1 97.7 89.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE CATALYTIC TRIAD OF THE ACTIVE CENTER
REMARK 800 CONSISTS OF THE RESIDUES SER 87 - HIS 285 - ASP 263, ALTHOUGH
REMARK 800 THEY ARE NOT EXPOSED TO THE SOLVENT.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 320
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1QGE SWS Q05489 1 - 39 NOT IN ATOMS LIST
REMARK 999
REMARK 999 REFERENCE: THE SEQUENCE FOR PSEUDOMONAS GLUMAE DESCRIBED
REMARK 999 IN FRENKEN ET AL. (1992), APPL. ENVIR. MICROBIOL. 58
REMARK 999 3787-3791; IS IDENTICAL TO THE AMINO ACID SEQUENCE OF
REMARK 999 CHROMOBACTERIUM VISCOSUM DESCRIBED IN SHIZUOKA ET AL.,
REMARK 999 1989 (GERMAN PATENT 3908131 A1).
DBREF 1QGE D 1 222 UNP Q05489 LIP_BURGL 40 261
DBREF 1QGE E 223 319 UNP Q05489 LIP_BURGL 262 358
SEQRES 1 D 222 ALA ASP THR TYR ALA ALA THR ARG TYR PRO VAL ILE LEU
SEQRES 2 D 222 VAL HIS GLY LEU ALA GLY THR ASP LYS PHE ALA ASN VAL
SEQRES 3 D 222 VAL ASP TYR TRP TYR GLY ILE GLN SER ASP LEU GLN SER
SEQRES 4 D 222 HIS GLY ALA LYS VAL TYR VAL ALA ASN LEU SER GLY PHE
SEQRES 5 D 222 GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU
SEQRES 6 D 222 LEU ALA TYR VAL LYS GLN VAL LEU ALA ALA THR GLY ALA
SEQRES 7 D 222 THR LYS VAL ASN LEU ILE GLY HIS SER GLN GLY GLY LEU
SEQRES 8 D 222 THR SER ARG TYR VAL ALA ALA VAL ALA PRO GLN LEU VAL
SEQRES 9 D 222 ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER
SEQRES 10 D 222 GLU PHE ALA ASP PHE VAL GLN ASP VAL LEU LYS THR ASP
SEQRES 11 D 222 PRO THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL
SEQRES 12 D 222 ASN VAL PHE GLY THR LEU VAL SER SER SER HIS ASN THR
SEQRES 13 D 222 ASP GLN ASP ALA LEU ALA ALA LEU ARG THR LEU THR THR
SEQRES 14 D 222 ALA GLN THR ALA THR TYR ASN ARG ASN PHE PRO SER ALA
SEQRES 15 D 222 GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA ALA
SEQRES 16 D 222 THR GLU THR VAL GLY GLY SER GLN HIS LEU LEU TYR SER
SEQRES 17 D 222 TRP GLY GLY THR ALA ILE GLN PRO THR SER THR VAL LEU
SEQRES 18 D 222 GLY
SEQRES 1 E 97 VAL VAL GLY ALA THR ASP THR SER THR GLY THR LEU ASP
SEQRES 2 E 97 VAL ALA ASN VAL THR ASP PRO SER THR LEU ALA LEU LEU
SEQRES 3 E 97 ALA THR GLY ALA VAL MET ILE ASN ARG ALA SER GLY GLN
SEQRES 4 E 97 ASN ASP GLY LEU VAL SER ARG CYS SER SER LEU PHE GLY
SEQRES 5 E 97 GLN VAL ILE SER THR SER TYR HIS TRP ASN HIS LEU ASP
SEQRES 6 E 97 GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA ASN ALA
SEQRES 7 E 97 GLU ASP PRO VAL ALA VAL ILE ARG THR HIS VAL ASN ARG
SEQRES 8 E 97 LEU LYS LEU GLN GLY VAL
HET CA E 320 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
FORMUL 4 HOH *324(H2 O)
HELIX 1 1 ILE D 33 HIS D 40 1 8
HELIX 2 2 ARG D 61 THR D 76 1 16
HELIX 3 3 SER D 87 VAL D 99 5 13
HELIX 4 4 PRO D 101 LEU D 103 5 3
HELIX 5 5 GLU D 118 THR D 129 1 12
HELIX 6 6 THR D 137 LEU D 149 1 13
HELIX 7 7 THR D 156 LEU D 167 1 12
HELIX 8 8 THR D 169 ASN D 178 1 10
HELIX 9 9 VAL E 236 THR E 240 5 5
HELIX 10 10 PRO E 242 ARG E 257 1 16
HELIX 11 11 ARG E 268 SER E 271 1 4
HELIX 12 12 ASP E 287 ILE E 289 5 3
HELIX 13 13 PRO E 303 GLN E 317 1 15
SHEET 1 A 6 VAL D 44 VAL D 46 0
SHEET 2 A 6 PRO D 10 VAL D 14 1 N VAL D 11 O TYR D 45
SHEET 3 A 6 VAL D 81 HIS D 86 1 N ASN D 82 O PRO D 10
SHEET 4 A 6 VAL D 104 ILE D 110 1 N ALA D 105 O VAL D 81
SHEET 5 A 6 GLN D 203 TRP D 209 1 N LEU D 205 O VAL D 107
SHEET 6 A 6 THR D 196 THR D 198 -1 N GLU D 197 O HIS D 204
SSBOND 1 CYS D 190 CYS E 269 1555 1555 2.02
LINK OD2 ASP E 241 CA CA E 320 1555 1555 2.40
LINK OD1 ASP E 287 CA CA E 320 1555 1555 2.57
LINK O GLN E 291 CA CA E 320 1555 1555 2.61
LINK O VAL E 295 CA CA E 320 1555 1555 2.45
LINK CA CA E 320 O HOH E 321 1555 1555 2.50
LINK CA CA E 320 O HOH E 330 1555 1555 2.37
SITE 1 ACT 3 SER D 87 HIS E 285 ASP E 263
SITE 1 AC1 6 ASP E 241 ASP E 287 GLN E 291 VAL E 295
SITE 2 AC1 6 HOH E 321 HOH E 330
CRYST1 40.980 43.350 140.690 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.024402 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023068 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007108 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
